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ABL1 — JAK2

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Hprd Interaction: JAK2 — ABL1 (in vitro) Xie et al., Oncogene 2001*, Argetsinger et al., Mol Cell Biol 2004, Feng et al., Mol Cell Biol 1997
• IRef Hprd Interaction: JAK2 — ABL1 (in vivo) Xie et al., Oncogene 2001*, Argetsinger et al., Mol Cell Biol 2004, Feng et al., Mol Cell Biol 1997

Text-mined interactions from Literome

Xie et al., Oncogene 2001 : Moreover, tyrosine phosphorylation of Jak2 by Bcr-Abl was inhibited by the Abl tyrosine kinase inhibitor, STI 571, in a dose dependent manner
Xie et al., Oncogene 2002 (Leukemia, Myelogenous, Chronic, BCR-ABL Positive) : Since the Jak2 binds to the C-terminal domain of Bcr-Abl and optimal Jak2 activation requires the SH2 domain, we tested whether Jak2 was involved in c-Myc protein induction by Bcr-Abl
Limnander et al., Mol Cell 2004 (Cell Transformation, Neoplastic) : SOCS-1 is expressed in v-Abl transformed cells but is unable to inhibit v-Abl mediated Jak-Stat signaling
Zhou et al., J Exp Med 2008 (Cell Transformation, Neoplastic...) : Interestingly, coexpression of Ahi-1 in BCR-ABL-inducible cells reverses growth deficiencies exhibited by BCR-ABL down-regulation and is associated with sustained phosphorylation of BCR-ABL and enhanced activation of JAK2-STAT5
Samanta et al., Leukemia 2011 (Leukemia, Myelogenous, Chronic, BCR-ABL Positive) : Janus kinase 2 regulates Bcr-Abl signaling in chronic myeloid leukemia ... Knocking down Jak2 in Bcr-Abl+ cells reduced levels of the Bcr-Abl protein and also the phosphorylation of Tyr177 of Bcr-Abl, and Jak2 overexpression rescued these knockdown effects ... Importantly, Jak2 inhibition decreased pTyr177 Bcr-Abl in immune complexes but did not reduce levels of Bcr-Abl , suggesting that the reduction of Bcr-Abl by Jak2 inhibition is a separate event from phosphorylation of Tyr177
Wilson-Rawls et al., Leukemia 1997 : P210 Bcr-Abl interacts with the interleukin-3 beta c subunit and constitutively activates Jak2